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10.1038/nsmb.3120 http://scihub22266oqcxt.onion/10.1038/nsmb.3120 C4675090!4675090!26551077     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26551077.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Struct+Mol+Biol 2015 ; 22 (12): 991-8 Nephropedia Template TP {{tp|p=26551077|t=2015. The role of lipids in mechanosensation |pdf=|usr=}}{{26551077}} gab.com Text The role of lipids in mechanosensation JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26551077 #FOAvip The ability of proteins to sense membrane tension is pervasive in biology. A higher resolution structure of E. coli MscS, the channel of small conductance, identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chain within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (two acyl chains) from MscS pockets and trigger channel opening. We propose the extent of acyl chain interdigitation in these pockets determines the conformation of MscS. Where interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable and the channel gates. Twit Text FOAVip The role of lipids in mechanosensation ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26551077 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26551077 #FOAvip English Wikipedia <ref>{{Cite pmid|26551077}}</ref> The role of lipids in mechanosensation #MMPMID26551077 Pliotas C; Dahl ACE; Rasmussen T; Mahendran KR; Smith TK; Marius P; Gault J; Banda T; Rasmussen A; Miller S; Robinson CV; Bayley H; Sansom MSP; Booth IR; Naismith JH Nat Struct Mol Biol 2015[Dec]; 22 (12): 991-8 PMID26551077show ga The ability of proteins to sense membrane tension is pervasive in biology. A higher resolution structure of E. coli MscS, the channel of small conductance, identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chain within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (two acyl chains) from MscS pockets and trigger channel opening. We propose the extent of acyl chain interdigitation in these pockets determines the conformation of MscS. Where interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable and the channel gates. äThe role of lipids in mechanosensation (epmc).pdf DeepDyve Pubget Overpricing